| | 1 | Author
| H. Newesely, R. Hosemann, B. U. Ther | Requires cookie* | | | Title
| Kollagen-Einschlußverbindungen Inclusion Compounds of Collagen  | | | | Abstract
| Small angle X-ray diagrams o f native collagen o f rat tail treated with phospho tungstic acid or mercury chloride or cobalt-and uranyl-nitrate, osmiumoxide or hydroxy apatite show the same characteristic new reflections and reflection lines. The only remarkable difference exists between fibers treated under stress or relaxed. These experiments give new evidence for the paracrystallini-ty of collagen. More than 1 0 0 parallel aligned ca. 40 A thick octafibrils consist o f 670 A long micro paracrystals with 5 ca. 25 A thick soft segment layers. In these soft segments the holes o f the octafi brils build up a lattice o f vacancies with lattice cells o f 38,5x35x135 A3 length. The above mention ed molecules penetrate from the lateral sides through the soft segments into these vacancies build ing up complexes with peptide groups of collagen. Under stress only a small amount o f vacancies is occupied, statistically distributed over the vacancy-lattice, because the soft segments of the octa fibrils are constricted. Without stress about 10 to 25% o f the octafibrils within one paracrystal are filled up with sediments in the soft regions. With increasing precipitation finally 500 A long nee dles are formed of the inclusive material as detected by Höhling with the electron microscope in collagen of turkey tendon. The importance o f the paracrystalline collagen model is emphasized to understand the biological process like the mineralisation o f collagen and ^-keratin in organism or the activity of bone apatite in exchanging calcium ions. | | | |
Reference
| Z. Naturforsch. 35c, 177—187 (1980) | | | |
Published
| 1980 | | | |
Keywords
| Microparacrystals, Calcification, Octafibrils, Hydroxyl Apatite, Collagen Inclusion Compounds | | | |
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| default:Reihe_C/35/ZNC-1980-35c-0177.pdf | | | | Identifier
| ZNC-1980-35c-0177 | | | | Volume
| 35 | |
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